1.4.1.20: phenylalanine dehydrogenase
This is an abbreviated version!
For detailed information about phenylalanine dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.20
Reaction
Synonyms
dehydrogenase, phenylalanine, L-PheDH, L-phenylalanine dehydrogenase, L-phenylalanine:NAD+ oxidoreductase, deaminating, PDH, PHD, PheDH, phenylalanine dehydrogenase, recombinant PheDH, recombinant phenylalanine dehydrogenase
ECTree
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results (Engineering
Engineering on EC 1.4.1.20 - phenylalanine dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
V144D
mutantion significantly reduces kcat value and also decreases Km value for phenylalanine relative to that of wild-type
V144L
mutation considerably increases specific activity toward phenylalanine and decreases toward L-tyrosine. ThePhe/Tyr specificity constant in V144L increases more than 4fold
V144N
mutation reduces the specific activity toward phenylalanine and increases toward tyrosine
D209G/Q18H/I336F
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mutant named 1stA7/1stB6, active with DL-propargylglycine
F110Y/G124C/G293A
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mutant named H14A12, active with DL-propargylglycine
G124A
G124A/L307V
K224Q/L283F/E313G
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mutant named 2ndB10/H7H10, active with DL-propargylglycine
L307V
N145A
N145L
N145V
Q18H/I336F/E313G
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mutant named 1stB6/H7H10, active with DL-propargylglycine
V135I/I308N/Q363H
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mutant named H21D1, active with DL-propargylglycine
V33A/A206D/L283F
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mutant named 2ndC2., active with DL-propargylglycine
K66Q/S149G/N262C
the mutant shows activity with phenylacetone and 4-phenyl-2-butanone
F124M/V125S/H126I/A127I/A128Y/R129Q
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the catalytic efficiencies of the mutant enzyme with aliphatic amino acids and aliphatic keto acids as substrates are 0.5% to 2% of that of the wild-type enzyme. The efficiencies for L-Phe and phenylpyruvate decreases to 0.0008% and 0.035% of that of the wild-type enzyme, respectively. Enzyme exists as monomeric or dimeric form, compared to wild-type enzyme which exists as hexameric enzyme form. Thermostability is lowered by mutation
K173A
-
37°C, t1/2 of the mutant enzyme is 60 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor
K69A
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37°C, t1/2 of the mutant enzyme is 50 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Km-value for L-Phe is 1400fold higher compared to wild type enzyme, Km-value for phenylpyruvate is 128fold higher compared to wild type enzyme. Turnover number for deamination is 686fold lower than that of wild-type enzyme, turnover-number for amination is 43fold lower than that of wild-type enzyme
K69A/K81A
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37°C, t1/2 of the mutant enzyme is 450 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Km-value for L-Phe is 200fold higher compared to wild type enzyme, Km-value for phenylpyruvate is 108fold higher compared to wild type enzyme. Turnover number for deamination is 110fold lower than that of wild-type enzyme, turnover-number for amination is 61fold lower than that of wild-type enzyme
K81A
-
37°C, t1/2 of the mutant enzyme is 38 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Turnover number for deamination is 440fold lower than that of wild-type enzyme, turnover-number for amination is 42fold lower than that of wild-type enzyme
K89A
-
37°C, t1/2 of the mutant enzyme is 75 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor
K90A
-
37°C, t1/2 of the mutant enzyme is 80 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor
R272M/E331Q/E196N
mutant with improved capability of catalyzing 2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid to the corresponding non-natural amino acid (S)-3-hydroxyadamantylglycine which is the key intermediate of saxagliptin
additional information
G124A
-
mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type
G124A/L307V
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mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type
L307V
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mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type
L307V
-
shows enhanced pH stability compared to the wild type enzyme
N145A
-
reduced activity with phenylpyruvate, improved activity with non-natural 2-oxo acid substrates
N145A
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the immobilised biocatalyst is remarkably robust, even in the presence of high concentrations of polar or non-polar organic solvents such as acetone, methanol, n-hexane, toluene and methylene chloride
N145A
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4-trifluoromethyl-phenylpyruvate is the preferred substrate, the reaction velocity at elevated substrate concentration (5 mM) is almost 10 times higher compared to the wild type enzyme
N145A
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shows enhanced pH stability compared to the wild type enzyme
N145L
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22% of wild-type activity with phenylpyruvate, improved activity with non-natural 2-oxo acid substrates
N145V
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reduced activity with phenylpyruvate, improved activity with non-natural 2-oxo acid substrates
additional information
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covalent immobilization of phenylalanine dehydrogenase onto commercially available enzyme carrier Eupergit CM for the synthesis of unnatural amino acid (S)-2-amino-4-phenylbutyric acid, method optimization and evaluation, overview. The immobilized enzyme shows increased thermostability, activity, broadened pH optimum, and remarkable improvement in operability and storage stability compared to the native enzyme. Immobilized PheDH is successfully applied for the synthesis of (S)-2-amino-4-phenylbutyric acid, achieving enantiomeric excess of more than 99% and yield of more than 80%; comparable to synthesis using the free PheDH
additional information
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covalent immobilization of phenylalanine dehydrogenase onto commercially available enzyme carrier Eupergit CM for the synthesis of unnatural amino acid (S)-2-amino-4-phenylbutyric acid, method optimization and evaluation, overview. The immobilized enzyme shows increased thermostability, activity, broadened pH optimum, and remarkable improvement in operability and storage stability compared to the native enzyme. Immobilized PheDH is successfully applied for the synthesis of (S)-2-amino-4-phenylbutyric acid, achieving enantiomeric excess of more than 99% and yield of more than 80%; comparable to synthesis using the free PheDH
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additional information
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the enzyme is modified initially with 2-amino-4,6-dichloro-s-triazine, and immobilized by hexamethylenediamine and glutaraldehyde. The highest activity of immobilized PheDH is determined as 95.75 U/g support with 56% retained activity. The optimum pH value of immobilized L-PheDH was shifted from pH 10.4 to pH 11.0. pH and thermal stability of the immobilized L-PheDH are improved compared to the native enzyme
additional information
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construction of a chimeric enzyme consisting of the N-terminal domain of Thermoactinomyces intermedius phenylalanine dehydrogenase, containing the substrate-binding region and the C-terminal domain of leucine dehydrogenase from Bacillus stearothermophilus containing the NAD+-binding region. The chimeric enzyme has a specific activity of 6% of that of the parental phenylalanine dehydrogenase and shows a broad substrate specificity in the oxidative deamination, like phenylalanine dehydrogenase. However, it acts much more effectively than phenylalanine dehydrogenase on Ile and Val
